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Recombinant Human Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (PDHB)

Recombinant Human Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (PDHB) — Together with PDHA1 forms the heterotetrameric E1 subunit of the pyruvate dehydrogenase (PDH) complex. Purity >90%.

SKU: BCRECP-001363 Categories: ,

Product Specifications

Product SkuBCRECP-001363
Product DescriptionRecombinant Human Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (PDHB) Protein is expressed from E.coli with N-terminal 6xHis-tagged. It contains 31-359aa. [Accession | P11177].
Uniprot No.P11177
Gene NamesPDHB
PurityGreater than 90% as determined by SDS-PAGE.
Expression SystemE.coli
Expression Region31-359aa
SpeciesHomo sapiens (Human)
Tag InfoN-terminal 6xHis-tagged
Molecular weight41.9kDa
ActivityPlease contact us to obtain bioactivity data.
BufferIf the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
StorageStore at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Research AreasCancer

Function

Together with PDHA1 forms the heterotetrameric E1 subunit of the pyruvate dehydrogenase (PDH) complex. The PDH complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (Probable). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) (Probable).

Biological Context

Subcellular Location: Mitochondrion matrix
Disease Association: Pyruvate dehydrogenase E1-beta deficiency (PDHBD) : An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis. [The disease is caused by variants affecting the gene represented in this entry]

Product Specifications

Recombinant Human Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (PDHB) is a recombinant protein from Homo sapiens (Human), expressed in E.coli, covering amino acids 31-359aa, with N-terminal 6xHis-tagged tag, molecular weight 41.9kDa, purity Greater than 90% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.

Recommended applications depend on the target, product format, and product-specific validation data. Refer to the product datasheet or Certificate of Analysis (CoA), or contact BioCrest Sci for application guidance.

Biological Activity: Please contact us to obtain bioactivity data.

Storage: Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shipping & Lead Time: Availability, shipping conditions, and estimated lead time are confirmed in the formal quotation or order confirmation based on the product format, destination, and order requirements.

Protein Biology

Function

Together with PDHA1 forms the heterotetrameric E1 subunit of the pyruvate dehydrogenase (PDH) complex (PubMed:17474719, PubMed:19081061). The PDH complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (Probable). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) (Probable). The E1 subunit catalyzes both the thiamine pyrophosphate (TPP)-dependent decarboxylation of pyruvate and the reductive acetylation of a lipoyl group covalently linked to the lipoyl-bearing domains of E2 (PubMed:19081061)

Subcellular Location

Mitochondrion matrix

Disease Association

Pyruvate dehydrogenase E1-beta deficiency (PDHBD) : An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis. [The disease is caused by variants affecting the gene represented in this entry]

Subunit

Heterotetramer of two PDHA1 and two PDHB subunits (PubMed:12651851, PubMed:17474719, PubMed:19081061, PubMed:29970614). The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase (PDH) complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3) (PubMed:14638692). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (PubMed:14638692). Interacts with DLAT (PubMed:20160912)

Gene: PDHB  |  Organism: Homo sapiens
Key Publications

Frequently Asked Questions

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Submit the Online Inquiry form with your required quantity and specifications, or email sales@biocrestsci.com. Available sizes, pricing, stock status, documentation, and estimated lead time are confirmed in the formal quotation.

What is the shipping and delivery time?

Availability, dispatch timing, shipping conditions, and delivery estimates depend on the product format, destination, and order requirements. These details are confirmed in the formal quotation or order confirmation.

How should this product be stored?

Follow the storage and handling instructions in the product-specific datasheet and Certificate of Analysis (CoA). Requirements may vary by product form and formulation; contact BioCrest Sci if product-specific guidance is needed.

What quality controls are performed on your products?

Quality-control data such as identity, purity, endotoxin level, or biological activity are provided only when specified on this product page, the datasheet, or Certificate of Analysis (CoA). Biological activity is not implied unless explicitly stated.

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